Integrated support for RIPTAC discovery, from ternary-complex modeling to biochemical, biophysical, and cellular validation.
ICE Bioscience provides a connected workflow that combines in silico design, orthogonal assay development, target-engagement analysis, and downstream functional evaluation to support more informed RIPTAC program decisions.
RIPTACs, or Regulated Induced Proximity Targeting Chimeras, are bifunctional molecules designed to bring a tumor-selective target protein into proximity with a pan-essential protein. In target-positive cells, this induced proximity can disrupt essential protein function and drive selective cancer-cell killing while sparing healthy cells with low or absent target expression.
As an emerging induced-proximity modality, RIPTAC discovery requires more than routine assay execution. Productive programs depend on ternary-complex hypothesis generation, structure-informed design, orthogonal validation, and biologically meaningful downstream readouts.

Structure-guided RIPTAC design supported by docking, pose comparison, and molecular-dynamics analysis to prioritize productive ternary-complex hypotheses for downstream testing.
Biophysical and biochemical assays characterize binary binding, ternary-complex formation, and mechanism-related activity through formats including HTRF, TR-FRET, SPR, and spectral shift.
Cell-based target engagement and functional readouts connect ternary-complex biology to pharmacological outcome, with additional support for safety panels, ADME, PK/PD, and selected in vivo studies.
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